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interleukin-8 (IL8; neutrophil-activating protein 1) 406 interleukin-8 (IL8; neutrophil-activating protein 1)
promotes lymphopoiesis, governing stem cell differentiation
into early pre-T and -B cells. It is also formed by thymic
stroma and promotes the growth and activation of T cells
and activates macrophages. It enhances fetal and adult
thymocyte proliferation. Thus, IL7 has a significant role for
proliferation during selected stages of B cell maturation, T
and NK cell survival, development, and homeostasis.
interleukin-8 (IL8; neutrophil-activating protein 1)
A chemokine 8-kDa protein of 72 residues produced by
macrophages, epithelial cells, and endothelial cells. Innate
immune system Toll-like receptors recognize antigen
patterns such as lipopolysaccharides in Gram-negative
bacteria. A cascade of biochemical reactions leads to the
secretion of IL8, a significant mediator of innate immune
system responses. The gene encoding this protein is a
member of the CXC chemokine family, which is one of the
principal mediators of the inflammatory response. This
chemokine is secreted by various cell types and acts as a
chemoattractant and also a powerful angiogenic factor. This
gene is critical in the pathogenesis of viral-induced bronchiolitis.
It and ten other members of the CXC chemokine gene
family form a chemokine gene cluster mapped to chromosome
4q. Any innate immune system cells bearing Toll-like
receptors can secrete IL8, whose primary function is to
recruit neutrophils to phagocytize antigen, which activates
the antigen pattern Toll-like receptors. It has a powerful
chemotactic effect on T lymphocytes and neutrophils and
Interleukin-8.
Interleukin-8.
upregulates the binding properties of leukocyte adhesion
receptor CD11b/CD18. IL8 is released from macrophages
processing antigen and is one of the chemokines designed
to signal other immune cells to a site of inflammation.
Its ability to attract neutrophils to sites of inflammation
makes it also known as neutrophil chemotactic factor. IL8
regulates expression of its own receptor on neutrophils and
has antiviral, immunomodulatory, and antiproliferative
properties. It prevents adhesion of neutrophils to endothelial
cells activated by cytokines, thereby blocking neutrophilmediated
injury. It participates in inflammation and the
migration of cells and facilitates neutrophil adherence to
endothelial cells through the induction of β 2 integrins by
neutrophils. Pregnant females with elevated IL8 levels face
increased risk of bearing offspring with schizophrenia. It
is the prototypic and most widely investigated chemokine.
Its powerful neutrophil chemotactic action makes IL8 a
primary regulatory molecule of acute inflammation. High
affinity neutralizing anti-IL8 antibodies have been used to
reveal the regulatory action of IL8 on neutrophil infiltration
into tissues. IL8 also has a second significant effect in
promoting angiogenesis. It contains the ELR motif that is
crucial to the chemotactic action of several α chemokine
family members. Monocytes, macrophages, CD4 + , CD8 + ,
and CD45RA + lymphocytes, among many other cell types
Schematic representation of the interleukin-8 (IL-8) receptor, which may be
of either high or low affinity. These receptors are seven transmembrane spanning
and are G-protein linked. They belong to the rhodopsin superfamily.
Whereas the high-affinity receptor binds IL-8 exclusively, the low affinity
receptor also shows specificity for NAP-2 and GRO/MPSA.